Q6NJJ2 (GSA_CORDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase
Short name=GSA
EC=5.4.3.8

Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name=GSA-AT

Gene names

Name:	hemL
Ordered Locus Names:	DIP0409

Organism

Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) [Complete proteome] [HAMAP]

Taxonomic identifier

257309 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › Corynebacterium diphtheriae

Protein attributes

Sequence length	430 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	(S)-4-amino-5-oxopentanoate = 5-aminolevulinate. HAMAP-Rule MF_00375
Cofactor	Pyridoxal phosphate By similarity. HAMAP-Rule MF_00375
Pathway	Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. HAMAP-Rule MF_00375
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_00375
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00375.
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.

Ontologies

Keywords
Biological process	Porphyrin biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Isomerase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glutamate-1-semialdehyde 2,1-aminomutase activity Inferred from electronic annotation. Source: UniProtKB-HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transaminase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 430	430	Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375		PRO_0000120404
Amino acid modifications
	Modified residue	267	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6NJJ2 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 6B94BAA04DD5DE16	FASTA	430	45,362
	10 20 30 40 50 60 MTSTQRSQEL FARAQQFTPG GVNSPVRAFG SVGGHARFIQ SAKGSKLYDV DGNEYVDLVC 70 80 90 100 110 120 SWGPMLLGNA HPEIVEAVQK AATNGLSFGA PTEAEVKIAE MIVDRTSVEE VRMVNSGTEA 130 140 150 160 170 180 TMSAVRLARG FTGRPKVIKF DGCYHGHVDA LLASAGSGVA TFALPDSPGV TGASAADTIV 190 200 210 220 230 240 VPYNDSEAVR AAFEAHPDQI ACVIAEAAAG NMGTVAPQDN FNAKLKEVAH EHGALLILDE 250 260 270 280 290 300 VMTGFRTSYN GWYGVDGVAG DLTTFGKVIS GGLPAAAFGG RADIMRYLAP EGPVYQAGTL 310 320 330 340 350 360 SGNPVAMAAG MKSLELATPE VYDMVRANAD RLAGLLHEAL DREGVAHHIQ RAATMLSVRF 370 380 390 400 410 420 AEGEGHNFDD MKAADTFRFP AFFHALLDNG IYASPSVFET WFVSAALTDD DFDKIEKALR 430 PAAQAAGKAK

References

[1]

"The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129." Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D., De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K., Moule S. , Quail M.A., Rabbinowitsch E., Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G., Parkhill J. Nucleic Acids Res. 31:6516-6523(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700971 / NCTC 13129 / Biotype gravis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248355 Genomic DNA. Translation: CAE48913.1.
RefSeq	NP_938790.1. NC_002935.2.
3D structure databases
ProteinModelPortal	Q6NJJ2.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
STRING	257309.DIP0409.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAE48913; CAE48913; DIP0409.
GeneID	2649362.
KEGG	cdi:DIP0409.
PATRIC	21481975. VBICorDip47633_0392.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0001.
HOGENOM	HOG000020210.
KO	K01845.
OMA	RFMVSGN.
OrthoDB	EOG6QVRHN.
Enzyme and pathway databases
UniPathway	UPA00251; UER00317.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 2 hits.
HAMAP	MF_00375. HemL_aminotrans_3.
InterPro	IPR004639. 4pyrrol_synth_GluAld_NH2Trfase. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
PANTHER	PTHR11986. PTHR11986. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
PIRSF	PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAM	SSF53383. SSF53383. 1 hit.
TIGRFAMs	TIGR00713. hemL. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSA_CORDI

Accession

Primary (citable) accession number: Q6NJJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	July 5, 2004
Last modified:	May 14, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program